Residual error Resonance

The five room-temperature and two liquid-nitrogen temperature data sets obtained in these experiments were reanalyzed by Cummings and Hart (1988). Where necessary, they introduced improved corrections for residual strain, resonance, and nuclear scattering to arrive at a set of mean structure-factor values with typical errors of 3-5 millielectrons. This is extremely good, but as noted, for some reflections the errors are significantly larger than the 0.1% claimed earlier. Additional accurate values for individual reflections are available for y-ray (Alkire et al. 1982), X-ray (Roberto and Batterman 1970, Trucano and Batterman 1972), and synchrotron X-ray (Tischler 1983, Tischler and Batterman 1984), measurements. Combined, these measurements provide a superbly accurate set for analysis of the charge density in silicon. 

Fig. 9 (continued) assignments of correlations from the complex are not available, (b) Residues whose resonances are affected by the IIS interaction are mapped on the proteasome structure, (c) Crystal structure of the llS-proteasome complex, (d) The intensities of resonances during the titration are used to obtain an approximate dissociation constant (irD = 12 10 pM) for the IIS interaction that is consistent with the core particle titration data (see insets). The decrease in intensity of one of the correlations from L81 is shown on the left and the concomitant increase in a bound peak on the right. Errors are quantified from signal-to-noise in spectra. [Ligand] and [Protein] refer to total ligand and protein concentrations. Adapted from [3] with permission... 

---